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National Repository of Grey Literature 1 records found  Search took 0.00 seconds. 
Microcalorimetry as a method to analyze protein interactions with ligands
 Durčák, Jindřich ; Konvalinka, Jan (advisor) ; Vaněk, Ondřej (referee)
The interactions of proteins with their binding partners occur in every living organisms, in almost every cell process. Therefore the exploration of protein interactions forms significant part of biochemical research. It appears that even more valuable information than the value of equilibrium constants of these interactions is determination of individual energy components - changes in enthalpy and entropy. Thermodynamic analysis by isothermal titration calorimetry (ITC) can determine the changes in entropy and enthalpy caused by formation of complex of binding partners. Microcalorimetry is also an important optimization technique in development of new drugs, for example antiretrovirotics. Despite HIV is a virus known for over 30 years, intensive research has neither brought vaccine nor drug that would permanently cure patients. Already 26 drugs were approved, most of them target viral enzymes reverse transcriptase and protease. Antiretroviral treatment prevents the propagation of HIV and maintains immune system, but long - term use leads to resistance against drugs, which is caused by mutations in the target proteins. One of relatively new targets of therapeutic intervention is capsid core formation of during assembly of new virions. During the assembly many protein - protein interactions take...
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